ID SYL_CAMJD Reviewed; 809 AA.
AC A7H2R6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049};
GN OrderedLocusNames=JJD26997_0632;
OS Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS 269.97).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT isolated from human blood.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000768; ABS43284.1; -; Genomic_DNA.
DR AlphaFoldDB; A7H2R6; -.
DR SMR; A7H2R6; -.
DR KEGG; cjd:JJD26997_0632; -.
DR HOGENOM; CLU_004427_0_0_7; -.
DR Proteomes; UP000002302; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 2.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..809
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009317"
FT MOTIF 40..50
FT /note="'HIGH' region"
FT MOTIF 579..583
FT /note="'KMSKS' region"
FT BINDING 582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 809 AA; 93268 MW; C537E7C634CEE377 CRC64;
MAYEASLIEK KWQKIWDENE YFEPKDDLNL PKKYILSMFP YPSGRIHMGH VRNYTIGDAL
ARYYRKIGFN VLHPIGFDSF GMPAENAAIK HKIHPKSWTY ENIAYMKKEL FSLGFSFSKK
RMLATSDPLY TKFEQEIFIK MFEKGLIYTK EANVNWCEQD QTVLANEQVE DGKCWRCGHE
VVQKKMPGYY VKITAYAEKL LKDLEGLRDK WPNQVLTMQE NWIGKSEGLA FSLNLDEKSK
QKAKESSLEV FTTRADTIYG VSYVALAPEH KIVQNLLLQN LLNQDVLNKI KAIQNQSPRE
RQSSEKEGYF LGIYAIHPLS GEKIPLWVAN FVLSDYGSGA VMAVPAHDER DFEFAKKYNL
AIKQVIQTQE NLPYTQKLGK LIHSQEFDNL DCNEARLKII SQFEAKNIGK RVVNFKIRDW
GVSRQRYWGA PIPMIKCQSC GIAPQKLENL PITLPEDVQI TGEGNPLDKH PTWKNCICPK
CGKEAQKESD TLDTFFESSW YFARFASDEK TWQEKALDEK SVKYWMSVDQ YIGGIEHAIL
HLLYARFFQK ALRDLGYLTQ NEPFDRLLTQ GMVLKDGAKM SKSKGNVVDP DEIIEKYGAD
TARLFMLFAA PPAKELEWND DAVEGAYRFI CKLYDRAQNI KKGELVELKQ ENLNKEEKYA
RLKVYEALKK SEEVYHQSFA FNTLIAACME ALNALALCKN EALEQEAFYI ILNILEPIIP
HVCFELSEEL FKCKNFKKLE LKEEVFVKDT LNLAVSINGK KRAEFKISSS ASKEEILAFA
KENTAKWLEG KSIVKEIYVE GKLVNLVIK
//
